Engineering novel Lec1 glycosylation mutants in CHO-DUKX cells: molecular insights and effector modulation of N-acetylglucosaminyltransferase I. (Q38328602)

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English	Engineering novel Lec1 glycosylation mutants in CHO-DUKX cells: molecular insights and effector modulation of N-acetylglucosaminyltransferase I.	scientific article

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scholarly article

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Europe PubMed Central

2 September 2017

Engineering novel Lec1 glycosylation mutants in CHO-DUKX cells: molecular insights and effector modulation of N-acetylglucosaminyltransferase I. (English)

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Europe PubMed Central

2 September 2017

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author name string

Xiaotian Zhong

1

1 reference

Europe PubMed Central

2 September 2017

Cecilia Cooley

2

1 reference

Europe PubMed Central

2 September 2017

Nilufer Seth

3

1 reference

Europe PubMed Central

2 September 2017

Z Sean Juo

4

1 reference

Europe PubMed Central

2 September 2017

Ella Presman

5

1 reference

Europe PubMed Central

2 September 2017

Nicole Resendes

6

1 reference

Europe PubMed Central

2 September 2017

Ravi Kumar

7

1 reference

Europe PubMed Central

2 September 2017

Martin Allen

8

1 reference

Europe PubMed Central

2 September 2017

Lidia Mosyak

9

1 reference

Europe PubMed Central

2 September 2017

Mark Stahl

10

1 reference

Europe PubMed Central

2 September 2017

Will Somers

11

1 reference

Europe PubMed Central

2 September 2017

Ronald Kriz

12

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Europe PubMed Central

2 September 2017

publication date

2 February 2012

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Europe PubMed Central

2 September 2017

Biotechnology and Bioengineering

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Europe PubMed Central

2 September 2017

109

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Europe PubMed Central

2 September 2017

7

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Europe PubMed Central

2 September 2017

1723-1734

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Europe PubMed Central

2 September 2017

A time- and cost-efficient system for high-level protein production in mammalian cells

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Mammalian glycosylation mutants as tools for the analysis and reconstitution of protein transport

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Glycoprotein structural genomics: solving the glycosylation problem

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Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I.

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Fringe modulation of Jagged1-induced Notch signaling requires the action of beta 4galactosyltransferase-1

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Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI.

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Inhibition of hybrid- and complex-type glycosylation reveals the presence of the GlcNAc transferase I-independent fucosylation pathway

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Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1, 4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II.

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Double knockdown of alpha1,6-fucosyltransferase (FUT8) and GDP-mannose 4,6-dehydratase (GMD) in antibody-producing cells: a new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC

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Mice lacking N-acetylglucosaminyltransferase I activity die at mid-gestation, revealing an essential role for complex or hybrid N-linked carbohydrates

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Glycosylation as a strategy to improve antibody-based therapeutics

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Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types

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Clearance mechanism of a mannosylated antibody-enzyme fusion protein used in experimental cancer therapy.

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Assembly of asparagine-linked oligosaccharides

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Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation

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Cloning and expression of the murine gene and chromosomal location of the human gene encoding N-acetylglucosaminyltransferase I

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Effector functions of a monoclonal aglycosylated mouse IgG2a: binding and activation of complement component C1 and interaction with human monocyte Fc receptor

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Product-identification and substrate-specificity studies of the GDP-L-fucose:2-acetamido-2-deoxy-beta-D-glucoside (FUC goes to Asn-linked GlcNAc) 6-alpha-L-fucosyltransferase in a Golgi-rich fraction from porcine liver

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Collectins and viral infection.

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Highly efficient deletion of FUT8 in CHO cell lines using zinc-finger nucleases yields cells that produce completely nonfucosylated antibodies.

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Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans

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Fringe is a glycosyltransferase that modifies Notch

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Engineering Chinese hamster ovary cells to maximize effector function of produced antibodies using FUT8 siRNA.

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Defucosylated chimeric anti-CC chemokine receptor 4 IgG1 with enhanced antibody-dependent cellular cytotoxicity shows potent therapeutic activity to T-cell leukemia and lymphoma

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Cell engineering and cultivation of chinese hamster ovary (CHO) cells.

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Genetic defect in N-acetylglucosaminyltransferase I gene of a ricin-resistant baby hamster kidney mutant.

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Establishment of HIV-1 resistance in CD4+ T cells by genome editing using zinc-finger nucleases

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Molecular cloning and characterization of the mouse UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I gene.

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Glycosylation defect in Lec1 Chinese hamster ovary mutant is due to a point mutation in N-acetylglucosaminyltransferase I gene.

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Targeted gene knockout in mammalian cells by using engineered zinc-finger nucleases.

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Molecular cloning and expression of cDNA encoding the enzyme that controls conversion of high-mannose to hybrid and complex N-glycans: UDP-N-acetylglucosamine: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I

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The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity

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Chinese hamster ovary cells selected for resistance to the cytotoxicity of phytohemagglutinin are deficient in a UDP-N-acetylglucosamine--glycoprotein N-acetylglucosaminyltransferase activity

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Identifiers

10.1002/BIT.24448

1 reference

Europe PubMed Central

2 September 2017

1 reference

Europe PubMed Central

2 September 2017

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